ID   V2XAX7_MONRO            Unreviewed;      1156 AA.
AC   V2XAX7;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   SubName: Full=Vacuolar membrane protein {ECO:0000313|EMBL:ESK96348.1};
GN   ORFNames=Moror_7134 {ECO:0000313|EMBL:ESK96348.1};
OS   Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS   (Crinipellis roreri).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX   NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK96348.1, ECO:0000313|Proteomes:UP000017559};
RN   [1] {ECO:0000313|EMBL:ESK96348.1, ECO:0000313|Proteomes:UP000017559}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK96348.1,
RC   ECO:0000313|Proteomes:UP000017559};
RX   PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA   Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA   Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA   Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E., Shao J.,
RA   Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT   "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT   Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT   mechanisms of the biotrophic and necrotrophic phases.";
RL   BMC Genomics 15:164-164(2014).
CC   -!- SIMILARITY: Belongs to the VPS11 family.
CC       {ECO:0000256|ARBA:ARBA00007070}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ESK96348.1}.
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DR   EMBL; AWSO01000050; ESK96348.1; -; Genomic_DNA.
DR   RefSeq; XP_007844388.1; XM_007846197.1.
DR   AlphaFoldDB; V2XAX7; -.
DR   STRING; 1381753.V2XAX7; -.
DR   KEGG; mrr:Moror_7134; -.
DR   HOGENOM; CLU_001287_0_0_1; -.
DR   OrthoDB; 5491867at2759; -.
DR   Proteomes; UP000017559; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:UniProtKB-UniRule.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR   CDD; cd16688; RING-H2_Vps11; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   InterPro; IPR000547; Clathrin_H-chain/VPS_repeat.
DR   InterPro; IPR016528; VPS11.
DR   InterPro; IPR024763; VPS11_C.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001841; Znf_RING.
DR   PANTHER; PTHR23323; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN; 1.
DR   PANTHER; PTHR23323:SF24; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 11 HOMOLOG; 1.
DR   Pfam; PF12451; VPS11_C; 1.
DR   Pfam; PF17122; zf-C3H2C3; 1.
DR   PIRSF; PIRSF007860; VPS11; 3.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   PROSITE; PS50236; CHCR; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017559};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          1066..1101
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          187..210
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          723..747
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          814..844
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        723..744
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1156 AA;  126425 MW;  968AE302BBFD59E5 CRC64;
     MSTGISAPQW RQYPFFDKVT VRDVHDAAST PDVFKSAPEI STIASSSAGV IVADIHGSVH
     LLNRDFESIS SWVAHVGGRV THMVERKGIL VTLGEEDTVR SPLLKIWDLN QKDKRTTAPL
     LLRSVKVQLS NRPHPVTTLA LSATLSHLAI GLGDGTVLIY RHLDQALAAS STSLTAIPKP
     RVIHESPTEP VTGLGFREPT PAPAHDSKSK DKIENMADSN LYLFISTTNH VLVYQATGRG
     SGANASVVDE IGCGLGCATM DGGISALIHG ESLTTIQAGH ANIGKGMGGR DSGRVMFVAR
     EEALYMVGID GRGNCFAHEG LKASVQVHAA YLVIVSPPAV PSASAASATM RNIARAGDVE
     GEVTKVTVFD PANKLVVFTG TFIQGVRDVI TAPWGNLYVL ENNGELTHLS EKPTSAKLDM
     LYSRGFYSGA LTLARTHGLD ESSVADIHRQ YGDYLYSRGE YDASMSQYVK TLGHVKASYV
     IRKFLDAQRI HNLVTYLQEL HAQGLANSDH TTLLLNTYTK LKDVARLDSF IKTESKAKLR
     QQDKSDREEH DPEELPFDLD TAIRVCRQAG YFDHAGYLAK KYERHEEYLR IQIEDAERYA
     DALAYFRKLG VDAAESNLAR YGRALLANLP EETTQLLIDL CTSTGTNLEF IDTSAEDTPV
     SNVSAAGKIG AAAAGGASYL SYLSLNKGST TGQVSDTATI PAPSIKTVKA GDSSSIRDET
     ATMKNGEGTI NAGSVSGTPR TSSPPPTIAA APAPAVLAAS GLTATTIGTA RPPRVQPVKR
     LSPRLYFAHF VDHMEQFVVF LETVAKRRWD QSLDADTDSK VKSNGAANNG VVDSPVDEED
     TESEKKDQVA VWNTLLELYL TLPGVSATAT SPAQSEETLR DKAICILQSK DIPYDPTHAL
     ILCSSHGCTK GLVLLWEKMG MYEDVLRFWM DRDKEGVSEA SAEVVRHLRI YGPQHPHLYP
     LVLRFLTSSS ELLSRHKVDV KEVIEHIDKE GILPPLGVVQ ILSRNNVASV GLVKEWLIQR
     IKQEREEIQT DQEWMNSYRM ETAEKRKQVE ELSNPEHPKS FTVTRCSQCK GQLDLPSIHF
     MCNHSYHQRC LPDNDTECPN CAREHGVIRE IRRNNEHLAS QHDVFLSEVK EGGFKAVADA
     FSRGIFNVSR VEEAAV
//